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CTK3_SCHPO
ID   CTK3_SCHPO              Reviewed;         218 AA.
AC   Q9USJ8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=CTD kinase subunit gamma;
DE            Short=CTDK-I gamma subunit;
DE   AltName: Full=CTD kinase subunit 3;
GN   Name=ctk3 {ECO:0000250|UniProtKB:P46963}; ORFNames=SPCC4B3.08;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1] {ECO:0000312|EMBL:CAB60682.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2] {ECO:0000305}
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Subunit of the CTDK-I complex, which hyperphosphorylates the
CC       C-terminal heptapeptide repeat domain (CTD) of the largest RNA
CC       polymerase II subunit. As part of the CTDK-I complex, involved in RNA
CC       polymerase II transcriptional elongation and pre-mRNA 3'-end
CC       processing. Together with ctk2, required for ctk1/lsk1 CTD kinase
CC       activation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: CTDK-I consists of three subunits, ctk1/lsk1, ctk2/lsc1 and
CC       ctk3 (also called alpha, beta and gamma). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the CTK3 family. {ECO:0000305}.
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DR   EMBL; CU329672; CAB60682.1; -; Genomic_DNA.
DR   PIR; T50440; T50440.
DR   RefSeq; NP_588082.1; NM_001023074.2.
DR   PDB; 5CE7; X-ray; 2.00 A; A=1-140.
DR   PDBsum; 5CE7; -.
DR   AlphaFoldDB; Q9USJ8; -.
DR   SMR; Q9USJ8; -.
DR   BioGRID; 276116; 68.
DR   STRING; 4896.SPCC4B3.08.1; -.
DR   MaxQB; Q9USJ8; -.
DR   PaxDb; Q9USJ8; -.
DR   PRIDE; Q9USJ8; -.
DR   EnsemblFungi; SPCC4B3.08.1; SPCC4B3.08.1:pep; SPCC4B3.08.
DR   GeneID; 2539555; -.
DR   KEGG; spo:SPCC4B3.08; -.
DR   PomBase; SPCC4B3.08; -.
DR   VEuPathDB; FungiDB:SPCC4B3.08; -.
DR   eggNOG; ENOG502S1MK; Eukaryota.
DR   HOGENOM; CLU_051552_0_0_1; -.
DR   InParanoid; Q9USJ8; -.
DR   OMA; RENIWAI; -.
DR   PhylomeDB; Q9USJ8; -.
DR   BRENDA; 2.7.11.23; 5613.
DR   PRO; PR:Q9USJ8; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0070692; C:CTDK-1 complex; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005509; F:calcium ion binding; NAS:PomBase.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IBA:GO_Central.
DR   GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
DR   GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IC:PomBase.
DR   GO; GO:0023052; P:signaling; NAS:PomBase.
DR   Gene3D; 1.25.40.90; -; 1.
DR   InterPro; IPR006569; CID_dom.
DR   InterPro; IPR042326; Ctk3.
DR   InterPro; IPR024637; Ctk3_C.
DR   InterPro; IPR024638; Ctk3_N.
DR   InterPro; IPR008942; ENTH_VHS.
DR   PANTHER; PTHR28291; PTHR28291; 1.
DR   Pfam; PF12243; CTK3; 1.
DR   Pfam; PF12350; CTK3_C; 1.
DR   PROSITE; PS51391; CID; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; mRNA processing; Nucleus; Reference proteome;
KW   Transcription.
FT   CHAIN           1..218
FT                   /note="CTD kinase subunit gamma"
FT                   /id="PRO_0000338604"
FT   DOMAIN          2..138
FT                   /note="CID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT   REGION          137..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           3..14
FT                   /evidence="ECO:0007829|PDB:5CE7"
FT   HELIX           21..23
FT                   /evidence="ECO:0007829|PDB:5CE7"
FT   HELIX           25..33
FT                   /evidence="ECO:0007829|PDB:5CE7"
FT   HELIX           35..37
FT                   /evidence="ECO:0007829|PDB:5CE7"
FT   HELIX           38..51
FT                   /evidence="ECO:0007829|PDB:5CE7"
FT   HELIX           54..73
FT                   /evidence="ECO:0007829|PDB:5CE7"
FT   HELIX           80..86
FT                   /evidence="ECO:0007829|PDB:5CE7"
FT   HELIX           88..95
FT                   /evidence="ECO:0007829|PDB:5CE7"
FT   HELIX           100..118
FT                   /evidence="ECO:0007829|PDB:5CE7"
FT   HELIX           124..139
FT                   /evidence="ECO:0007829|PDB:5CE7"
SQ   SEQUENCE   218 AA;  24640 MW;  4AA0F1E5B24B842D CRC64;
     MDPFEGRMTF LQLLGKLNAS QFSQIKPAQF AIKHLDLEED LYSCIWEELE SGSFNTRVNI
     MYFVDTLCEM CLKNGLTGGY LNMISRDICK LVQNVAPIGA AGAANAPEVR KVLQSLHEKK
     VIDDNQYKDA MATVEAHEQA SKSGDTSTSG AISKNDILKR IEEDRERHKR MRENIWAISE
     PELEAEIAWN TTQGITESDL ESLKDEYEKF NECLHATS
 
 
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